ID A0A0X1SXY8_PSEAA Unreviewed; 832 AA.
AC A0A0X1SXY8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432, ECO:0000256|HAMAP-Rule:MF_00393};
DE Short=GPAT {ECO:0000256|HAMAP-Rule:MF_00393};
DE EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113, ECO:0000256|HAMAP-Rule:MF_00393};
GN Name=plsB {ECO:0000256|HAMAP-Rule:MF_00393};
GN ORFNames=AWM79_04080 {ECO:0000313|EMBL:AMB84530.1};
OS Pseudomonas agarici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB84530.1, ECO:0000313|Proteomes:UP000063229};
RN [1] {ECO:0000313|EMBL:AMB84530.1, ECO:0000313|Proteomes:UP000063229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB84530.1,
RC ECO:0000313|Proteomes:UP000063229};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000510, ECO:0000256|HAMAP-
CC Rule:MF_00393};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|HAMAP-Rule:MF_00393}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00393};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00393};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00393}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00393}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|HAMAP-Rule:MF_00393}.
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DR EMBL; CP014135; AMB84530.1; -; Genomic_DNA.
DR RefSeq; WP_060782200.1; NZ_CP014135.1.
DR AlphaFoldDB; A0A0X1SXY8; -.
DR STRING; 46677.AWM79_04080; -.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000063229; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR03703; plsB; 1.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500064; GPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00393};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00393}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00393};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00393};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00393};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00393};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00393};
KW Reference proteome {ECO:0000313|Proteomes:UP000063229};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00393}.
FT DOMAIN 304..431
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT MOTIF 309..314
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
SQ SEQUENCE 832 AA; 94525 MW; 7808195A148E4754 CRC64;
MTRSPFRRLA FGTLRRLLYL WVRSETINQS ALTLNLDRSR PVFYVLQSPS LTDLAVVDHE
CTRAGLPRPV LPVSVGSLME PAAFFYLTPD PDWLGRQDKR GAPPTLTRLV DALSQHAAED
TLIIPVSVFW GQSPDSESSP WKLLFADSWA VTGRLRRLLS ILILGRKTRV QFSAPIHLRD
LVEHNKGLER TVRMAQRILR VHFRHLKTAV IGPDLSHRRN LVKGLVNEPL VRQAILEQAQ
RENISTQKAK AQALRYGNEI ASDYTYTAIR FLEVVLSWFW NKIYDGIKVN HIEGVQAVAP
GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHIAAGINLN MPVIGSLLRR GGAFFMRRTF
KGNPLYTSVF NEYLHTLFTK GFPVEYFVEG GRSRTGRMLQ PKTGMLAITL RSFLRSSRTP
IVFVPVYIGY ERVLEGRTYL GELRGASKKK ESIFDIFKVI GALKQRFGQV AVNFGEPIKL
AEFLDQEQPD WRTQALGPQF KPAWLNATTH RLGERVARHL NEAAAINPVN LVALALLSTS
RLALDDRAMA RVLDLYLALL RRVPYSPHTT LPQGDGQALI RHVKEMDLLS EQSDALGKIL
YLDEQNAVLM TYYRNNVLHI FALPALLASF FQSSSRMSRE LILRYTRALY PYLQSELFIR
WSLDELDAVI DQWLEAFVEQ GLLRFENEVY LRPAPSSRHF VLLTLLSKSI AQTLQRFYMA
ISLLLNSGQS SISAEELEDL CTVMAQRLSI LHGLNAPEFF DKSLFRHFIQ TLLDLDVLRR
NEAGKLSYHE LLGELAEGAA KRVLPAQIRL SIRQVALHRS EDAADPQANL GE
//
